ID   BUR1_GIBZE              Reviewed;         473 AA.
AC   Q4I5U9;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2005, sequence version 1.
DT   16-JUN-2009, entry version 31.
DE   RecName: Full=Serine/threonine-protein kinase BUR1;
DE            EC=2.7.11.22;
DE            EC=2.7.11.23;
GN   Name=BUR1; ORFNames=FG07409;
OS   Gibberella zeae (Fusarium graminearum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Nectriaceae;
OC   Gibberella.
OX   NCBI_TaxID=5518;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PH-1 / NRRL 31084;
RX   PubMed=17823352; DOI=10.1126/science.1143708;
RA   Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G.,
RA   Di Pietro A., Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G.,
RA   Antoniw J., Baldwin T., Calvo S.E., Chang Y.-L., DeCaprio D.,
RA   Gale L.R., Gnerre S., Goswami R.S., Hammond-Kosack K., Harris L.J.,
RA   Hilburn K., Kennell J.C., Kroken S., Magnuson J.K., Mannhaupt G.,
RA   Mauceli E.W., Mewes H.-W., Mitterbauer R., Muehlbauer G.,
RA   Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T., Qi W.,
RA   Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA   Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT   "The Fusarium graminearum genome reveals a link between localized
RT   polymorphism and pathogen specialization.";
RL   Science 317:1400-1402(2007).
CC   -!- FUNCTION: Serine/threonine-protein kinase involved in
CC       transcription regulation. Phosphorylates the UBC2/RAD6 ubiquitin-
CC       conjugating enzyme (E2), leading to monoubiquitination of histone
CC       H2B and the silencing of telomeric-associated genes. Also required
CC       for histone H3 methylation. Necessary for the recovery from
CC       pheromone-induced growth arrest in the cell cycle G1 phase (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- CATALYTIC ACTIVITY: ATP + [DNA-directed RNA polymerase] = ADP +
CC       [DNA-directed RNA polymerase] phosphate.
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
CC       Ser/Thr protein kinase family. CDC2/CDKX subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   EMBL; AACM01000309; EAA76128.1; -; Genomic_DNA.
DR   RefSeq; XP_387585.1; -.
DR   GeneID; 2789242; -.
DR   KEGG; fgr:FG07409.1; -.
DR   BRENDA; 2.7.11.22; 74326.
DR   BRENDA; 2.7.11.23; 74326.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004693; F:cyclin-dependent protein kinase activity; IEA:EC.
DR   GO; GO:0008353; F:RNA polymerase subunit kinase activity; IEA:EC.
DR   GO; GO:0006468; P:protein amino acid phosphorylation; IEA:InterPro.
DR   InterPro; IPR000719; Prot_kinase_core.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_pkinase-rel.
DR   InterPro; IPR008271; Ser_thr_pkin_AS.
DR   InterPro; IPR002290; Ser_thr_pkinase.
DR   Pfam; PF00069; Pkinase; 1.
DR   ProDom; PD000001; Prot_kinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Nucleotide-binding; Nucleus;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1    473       Serine/threonine-protein kinase BUR1.
FT                                /FTId=PRO_0000085683.
FT   DOMAIN       37    339       Protein kinase.
FT   NP_BIND      43     51       ATP (By similarity).
FT   COMPBIAS    411    473       Arg-rich.
FT   ACT_SITE    169    169       Proton acceptor (By similarity).
FT   BINDING      66     66       ATP (By similarity).
SQ   SEQUENCE   473 AA;  54187 MW;  61CBCD21D9091F6C CRC64;
     MEKLSETTPN GTSPRTFALN HSRPRSSFKG CSRISDYELL GKLGEGTFGE VHRARLRKTG
     ALVALKKIIM HHEKDGFPIT ALREIKLLKL LSHKNILRLE DMAIEHPTRQ TDKRKKPIVY
     MATPYMDHDL SGLLDNPSVQ FKEPQIKCYM LQLLEGLRYL HDSRILHRDM KAANLLINNK
     GILQIADFGL ARHYDGRTPE SGVPMGEGKR DYTGLVVTRW YRPPELLLQL RQYTPAIDVW
     GVGCVFGEML YGKPILAGES DAAQLDIIWD LMGSPNEENM PRWKSLPGAD HLTPRPRTGN
     LETRFRQYGS GAVSLLKELL RLDWRTRINA VDALQHPWFK MQPLPLEPHE IPTYEESHEL
     DRRKFHDRKA ALPPAPKGGT VGVGPDANGA TAGFNSNEPY GNGRNGVNGG RRRDDRPPPP
     RDDRPPPRDD RRRRNSREDR RFDRDRGTMS RSRSPRHDRS RDRDRPDHNG YRR
//